LOCUS       NP_037309                430 aa            linear   ROD 27-APR-2025
DEFINITION  aspartate aminotransferase, mitochondrial [Rattus norvegicus].
ACCESSION   NP_037309
VERSION     NP_037309.1
DBSOURCE    REFSEQ: accession NM_013177.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Liu,X., Li,X. and Zhou,H.
  TITLE     Changes in glutamic oxaloacetic transaminase 2 during rat
            physiological and pathological cardiomyocyte hypertrophy
  JOURNAL   BMC Cardiovasc Disord 23 (1), 595 (2023)
   PUBMED   38053021
  REMARK    GeneRIF: Changes in glutamic oxaloacetic transaminase 2 during rat
            physiological and pathological cardiomyocyte hypertrophy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Xu,J., Khoury,N., Jackson,C.W., Escobar,I., Stegelmann,S.D.,
            Dave,K.R. and Perez-Pinzon,M.A.
  TITLE     Ischemic Neuroprotectant PKCepsilon Restores Mitochondrial
            Glutamate Oxaloacetate Transaminase in the Neuronal NADH Shuttle
            after Ischemic Injury
  JOURNAL   Transl Stroke Res 11 (3), 418-432 (2020)
   PUBMED   31473978
  REMARK    GeneRIF: Ischemic Neuroprotectant PKCepsilon Restores Mitochondrial
            Glutamate Oxaloacetate Transaminase in the Neuronal NADH Shuttle
            after Ischemic Injury.
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Zhang,Y., Kallenberg,C., Hyatt,H.W., Kavazis,A.N. and Hood,W.R.
  TITLE     Change in the Lipid Transport Capacity of the Liver and Blood
            during Reproduction in Rats
  JOURNAL   Front Physiol 8, 517 (2017)
   PUBMED   28798692
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Yang,L., Shen,Z.Y., Wang,R.R., Yin,M.L., Zheng,W.P., Wu,B., Liu,T.
            and Song,H.L.
  TITLE     Effects of heme oxygenase-1-modified bone marrow mesenchymal stem
            cells on microcirculation and energy metabolism following liver
            transplantation
  JOURNAL   World J Gastroenterol 23 (19), 3449-3467 (2017)
   PUBMED   28596681
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Rodriguez-Cruz,M., Gonzalez,R.S., Maldonado,J., Lopez-Alarcon,M.
            and Bernabe-Garcia,M.
  TITLE     The effect of gestational age on expression of genes involved in
            uptake, trafficking and synthesis of fatty acids in the rat
            placenta
  JOURNAL   Gene 591 (2), 403-410 (2016)
   PUBMED   27317891
REFERENCE   6  (residues 1 to 430)
  AUTHORS   von Deimling,O.H., Groning,J. and Gaa,A.
  TITLE     Genetic and biochemical characterization of a new chymotrypsin
            isozyme of the house mouse, CTRA-1
  JOURNAL   Biochem Genet 29 (11-12), 545-557 (1991)
   PUBMED   1820020
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Watazu,Y., Uji,Y., Sugiuchi,H., Okabe,H. and Murao,S.
  TITLE     New automated measurement of mitochondrial aspartate
            aminotransferase with use of protease 401
  JOURNAL   Clin Chem 36 (4), 687-689 (1990)
   PUBMED   2182221
REFERENCE   8  (residues 1 to 430)
  AUTHORS   White,R.A., Birkenmeier,C.S., Lux,S.E. and Barker,J.E.
  TITLE     Ankyrin and the hemolytic anemia mutation, nb, map to mouse
            chromosome 8: presence of the nb allele is associated with a
            truncated erythrocyte ankyrin
  JOURNAL   Proc Natl Acad Sci U S A 87 (8), 3117-3121 (1990)
   PUBMED   2139228
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Peters,J. and Nash,H.R.
  TITLE     Polymorphism of esterase 11 in Mus musculus, a further esterase
            locus on chromosome 8
  JOURNAL   Biochem Genet 15 (3-4), 217-226 (1977)
   PUBMED   869894
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Nichols,E.A. and Ruddle,F.H.
  TITLE     Polymorphism and linkage of glutathione reductase in Mus musculus
  JOURNAL   Biochem Genet 13 (5-6), 323-329 (1975)
   PUBMED   1180875
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM056810.1, BC061792.1 and CB607680.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M18467.1, BC061792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..430
                     /product="aspartate aminotransferase, mitochondrial"
                     /EC_number="2.6.1.1"
                     /EC_number="2.6.1.7"
                     /note="FABP-1; FABPpm; mAspAT; transaminase A; fatty
                     acid-binding protein; plasma membrane-associated fatty
                     acid-binding protein; Glutamate oxaloacetate transaminase
                     2, mitochondrial (aspartate aminotransferase 2);
                     glutamic-oxaloacetic transaminase 2, mitochondrial
                     (aspartate aminotransferase 2); kynurenine
                     aminotransferase 4; kynurenine aminotransferase IV;
                     kynurenine--oxoglutarate transaminase 4;
                     kynurenine--oxoglutarate transaminase IV"
                     /calculated_mol_wt=44526
     transit_peptide 1..29
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:17442055,
                     ECO:0000269|PubMed:7309704, ECO:0000269|PubMed:7470110,
                     ECO:0000269|PubMed:8238519; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
                     /calculated_mol_wt=2806
     mat_peptide     30..430
                     /product="Aspartate aminotransferase, mitochondrial.
                     /id=PRO_0000001218"
                     /note="propagated from UniProtKB/Swiss-Prot (P00507.2)"
                     /calculated_mol_wt=44526
     Region          32..430
                     /region_name="PLN02397"
                     /note="aspartate transaminase"
                     /db_xref="CDD:215222"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            107
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            122
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            order(133..135,162,215,246,276,278..279,287)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(136,172,239,285..287,323,326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            159
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            234
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            279
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     Site            296
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            313
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            338
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            345
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            387
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            396
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            404
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     CDS             1..430
                     /gene="Got2"
                     /gene_synonym="ASPATA; mAAT"
                     /coded_by="NM_013177.2:119..1411"
                     /db_xref="GeneID:25721"
                     /db_xref="RGD:2722"
ORIGIN      
        1 mallhsgrvl sgmaaafhpg laaaasaras swwthvemgp pdpilgvtea fkrdtnskkm
       61 nlgvgayrdd ngkpyvlpsv rkaeaqiagk nldkeylpig gladfckasa elalgensev
      121 lksgrfvtvq tisgtgalrv gasflqrffk fsrdvflpkp swgnhtpifr dagmqlqgyr
      181 yydpktcgfd fsgaledisk ipeqsvlllh acahnptgvd prpeqwkema avvkkknlfa
      241 ffdmayqgfa sgdgdkdawa vrhfieqgin vclcqsyakn mglygervga ftvvckdaee
      301 akrvesqlki lirplysnpp lngariaati ltspdlrkqw lqevkgmadr iismrtqlvs
      361 nlkkegsshn wqhitdqigm fcftglkpeq verltkefsv ymtkdgrisv agvtsgnvgy
      421 lahaihqvtk
//
